Crystalline Amino Acids

Болдырева, Е. В.

doi:10.1007/978-1-4020-5941-4_7

Cited by 31 publications

(30 citation statements)

References 163 publications

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“…The so-called 20 standard amino acids are fundamental building blocks of living systems [ 1 ]. They are usually obtained in solid form from aqueous solution by evaporation of the solvent [ 2 ]. Most of today’s knowledge about amino acids is therefore limited to the temperature and pressure range of liquid water.…”

Section: Introductionmentioning

confidence: 99%

Thermal decomposition of the amino acids glycine, cysteine, aspartic acid, asparagine, glutamic acid, glutamine, arginine and histidine

et al. 2018

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BackgroundThe pathways of thermal instability of amino acids have been unknown. New mass spectrometric data allow unequivocal quantitative identification of the decomposition products.ResultsCalorimetry, thermogravimetry and mass spectrometry were used to follow the thermal decomposition of the eight amino acids G, C, D, N, E, Q, R and H between 185 °C and 280 °C. Endothermic heats of decomposition between 72 and 151 kJ/mol are needed to form 12 to 70% volatile products. This process is neither melting nor sublimation. With exception of cysteine they emit mainly H2O, some NH3 and no CO2. Cysteine produces CO2 and little else. The reactions are described by polynomials, AA→a NH3+b H2O+c CO2+d H2S+e residue, with integer or half integer coefficients. The solid monomolecular residues are rich in peptide bonds.ConclusionsEight of the 20 standard amino acids decompose at well-defined, characteristic temperatures, in contrast to commonly accepted knowledge. Products of decomposition are simple. The novel quantitative results emphasize the impact of water and cyclic condensates with peptide bonds and put constraints on hypotheses of the origin, state and stability of amino acids in the range between 200 °C and 300 °C.

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Section: Introductionmentioning

confidence: 99%

Thermal decomposition of the amino acids glycine, cysteine, aspartic acid, asparagine, glutamic acid, glutamine, arginine and histidine

et al. 2018

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“…21 Several other review articles have also discussed various aspects of amino acids crystal structures. 22,23 However, to date, no attempts have been made to define the crystal packing of amino acids as layered structured materials, reminiscent of cross-β architecture, and the effects of such organizations on protein folding. Moreover, all the reported supramolecular β-Sheet structures comprise peptides, where amino acids are connected through amide bonds.…”

Section: Introduction 1synthetic and Biological Layered Structuresmentioning

confidence: 99%

“…In pioneer work, Görbitz carefully investigated amino acid crystal structures and provided important insights . Several other review articles have also discussed various aspects of amino acids crystal structures. , However, to date, no attempts have been made to define the crystal packing of amino acids as layered structured materials, reminiscent of cross-β architecture, and the effects of such organizations on protein folding. Moreover, all the reported supramolecular β-Sheet structures comprise peptides, where amino acids are connected through amide bonds.…”

Section: Introductionmentioning

confidence: 99%

Organization of Amino Acids into Layered Supramolecular Secondary Structures

et al. 2018

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The unique physiochemical properties and multiscale organization of layered materials draw the attention of researchers across a wide range of scientific disciplines. Layered structures are commonly found in diverse biological systems where they fulfill various functions. A prominent example of layered biological materials is the organization of proteins and polypeptides into the archetypal aggregated amyloidal structures. While the organization of proteins into amyloid structures was initially associated with various degenerative disorders, it was later revealed that proteins not related to any disease could also form identical layered assemblies. Thus, it appears that the ability of peptides and proteins to produce amyloid-like aggregates represents a generic property of polyamides to assemble into higher order fibrillar structures. In the aggregated state, the peptide backbone forms β-sheet structures which are further organized into layered arrangements. We have recently extended the identified amyloidogenic building blocks to include not only peptides or proteins, but also single amino acids and other metabolites. High resolution spectroscopy and crystallography analyses confirm the clear potential of amino acids and other metabolites to form layered amyloid-like aggregates showing biophysical and biochemical properties similar to protein amyloids. Therefore, the generic propensity of peptides and proteins backbones to assemble into layered organizations may emanate from their basic building block, the amino acid. In this Account, we aim to introduce the concept of supramolecular β-sheet organization of single amino acids and to present an analysis of their layered-structure organization based on single crystal structures. We demonstrate that, despite the different side-chains that considerably vary in their chemical properties, all coded amino acids display a layer-like assembly stabilized by α-amine to α-carboxyl H-bonds, resembling supramolecular β-sheet structures, while the side-chains determine the higher order organization of the layers. Our work presents the first analysis of the β-sheet propensity of single amino acids in their unbound form, indicating an evolutionary predisposition. We classify the amino acids β-sheet propensity on the basis of the interlayer separation distance in the crystal packing, which correlates well with previously reported classifications based on various criteria, such as hydrophobicity, steric bulkiness, and folding. In addition, we demonstrate that the relative direction of α-amine to α-carboxyl H-bonding pattern provides critical insights regarding the stabilization of parallel versus antiparallel β-sheet structures by the various amino acids. Taken together, our analysis of amino acid crystals provides substantial information regarding protein folding and dynamics and could serve as basic rules set for the design of potential building blocks for molecular self-assembly to produce functional materials of tunable properties, an important objective of bottom-up nanotechn...

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“…Apart from these rather special conditions, the aspect of seeding and even aging of solution ("solution memory") play important roles in the controlled growth of the desired polymorph. A discussion of the whole data would go beyond the scope of this book; for detailed information see, e.g., Li and Rodríguez-Hornedo (1992), Perlovich et al (2001), Boldyreva et al (2003a, b, c), Boldyreva (2008), Srinivasan et al (2011), as well as the references given above. A short summary of all these results can be given as follows.…”

Section: Glycinementioning

confidence: 97%

“…It was found that using seeds of this form taken from mixtures helps to obtain a higher yield. Boldyreva (2008) reported that spontaneous antisolvent precipitation with acetone from a solution of acetic acid yields the pure β-polymorph, but only if the solution has been left for about 3 days.…”

Section: Glycinementioning

confidence: 98%

Amino Acid Structures

Fleck

Petrosyan

2014

Salts of Amino Acids

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Although this book deals with salts of amino acids, this chapter discusses the structures of pristine amino acids, since these molecular structures are also found in salts, and factors as solubility and conditions of crystal growth are important for the synthesis of amino acid salts as well as the pure form. In this context, the impact of minimal changes in conditions (such as impurities) on the growth of amino acid crystals is noted. The structural variation is very high, as not only amino acids differ from each other, but many amino acids exist in more than one form. This refers to the fact that enantiopure crystals can be grown as well as racemates (so-called DL-amino acids). Moreover, often more than one hydration state is found: Anhydrous forms are common, but many amino acids form hydrated crystals. For some amino acids (e.g., glycine, proline, methionine), more than one polymorph of the same hydration state is found. Some of these polymorphs form at ambient condition, often due to minuscule changes in conditions. For others, variation in temperature and pressure has been found to be the cause of the formation of different polymorphs. High-pressure data are available for some amino acids (e.g., alanine, serine, cysteine). Most amino acids are found to form a so-called head-to-tail motif, where acid and amino groups connect to form infinite chains. In some of the larger, nonpolar amino acids, a bilayer pattern is found, where polar groups of opposing molecules face each other, forming a layer, with the hydrophobic side chain facing outward (this motif is found in phenylalanine, methionine, leucine, or isoleucine). Not all amino acids crystallize readily, as is proved by the crystal structure of L-arginine, which could be determined only very recently, and that of lysine, which could not be solved at all to date. In addition to the standard 20, some nonstandard amino acids are discussed. Finally, notes on remarkable physical effects (such as piezoelectric data) or possible applications (as for instance the interactions of amino acids with carbon nanotubes) are presented.

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Crystalline Amino Acids

Cited by 31 publications

References 163 publications

Thermal decomposition of the amino acids glycine, cysteine, aspartic acid, asparagine, glutamic acid, glutamine, arginine and histidine

Thermal decomposition of the amino acids glycine, cysteine, aspartic acid, asparagine, glutamic acid, glutamine, arginine and histidine

Organization of Amino Acids into Layered Supramolecular Secondary Structures

Amino Acid Structures

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